CA1266628A - Fabrication et expression de genes structuraux - Google Patents
Fabrication et expression de genes structurauxInfo
- Publication number
- CA1266628A CA1266628A CA000427371A CA427371A CA1266628A CA 1266628 A CA1266628 A CA 1266628A CA 000427371 A CA000427371 A CA 000427371A CA 427371 A CA427371 A CA 427371A CA 1266628 A CA1266628 A CA 1266628A
- Authority
- CA
- Canada
- Prior art keywords
- sequence
- duplex
- dna
- bases
- gene
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 143
- 230000014509 gene expression Effects 0.000 title claims abstract description 37
- 238000004519 manufacturing process Methods 0.000 title abstract description 30
- 108020004414 DNA Proteins 0.000 claims abstract description 81
- 102000053602 DNA Human genes 0.000 claims abstract description 78
- 238000000034 method Methods 0.000 claims abstract description 66
- 108020004705 Codon Proteins 0.000 claims abstract description 46
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 40
- 230000015572 biosynthetic process Effects 0.000 claims abstract description 33
- 150000001413 amino acids Chemical class 0.000 claims abstract description 31
- 238000003786 synthesis reaction Methods 0.000 claims abstract description 22
- 244000005700 microbiome Species 0.000 claims abstract description 15
- 238000002360 preparation method Methods 0.000 claims abstract description 13
- 230000000295 complement effect Effects 0.000 claims description 26
- 239000002773 nucleotide Substances 0.000 claims description 23
- 125000003729 nucleotide group Chemical group 0.000 claims description 19
- 239000000203 mixture Substances 0.000 claims description 11
- 239000011541 reaction mixture Substances 0.000 claims description 8
- 238000000137 annealing Methods 0.000 claims description 5
- 241000282414 Homo sapiens Species 0.000 abstract description 22
- 241000588724 Escherichia coli Species 0.000 abstract description 15
- 230000004927 fusion Effects 0.000 abstract description 8
- 238000006257 total synthesis reaction Methods 0.000 abstract description 2
- JMHFFDIMOUKDCZ-XKMGUCBZSA-N chembl2369948 Chemical compound C([C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@@H](CCSC)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)[C@@H](C)O)[C@@H](C)O)C(C)C)[C@@H](C)O)C1=CC=CC=C1 JMHFFDIMOUKDCZ-XKMGUCBZSA-N 0.000 abstract 2
- 235000018102 proteins Nutrition 0.000 description 32
- 102000004196 processed proteins & peptides Human genes 0.000 description 29
- 108090000765 processed proteins & peptides Proteins 0.000 description 29
- 235000001014 amino acid Nutrition 0.000 description 28
- 229940024606 amino acid Drugs 0.000 description 28
- 210000004027 cell Anatomy 0.000 description 28
- 229920001184 polypeptide Polymers 0.000 description 26
- 239000000047 product Substances 0.000 description 23
- 239000013598 vector Substances 0.000 description 23
- 108091028043 Nucleic acid sequence Proteins 0.000 description 17
- 239000013612 plasmid Substances 0.000 description 17
- 238000006243 chemical reaction Methods 0.000 description 15
- 230000009466 transformation Effects 0.000 description 15
- 238000005755 formation reaction Methods 0.000 description 12
- 239000012634 fragment Substances 0.000 description 11
- 108020004999 messenger RNA Proteins 0.000 description 11
- 108020004511 Recombinant DNA Proteins 0.000 description 10
- 238000007792 addition Methods 0.000 description 10
- 238000005304 joining Methods 0.000 description 10
- 239000000243 solution Substances 0.000 description 10
- 102100038796 E3 ubiquitin-protein ligase TRIM13 Human genes 0.000 description 8
- 101000664589 Homo sapiens E3 ubiquitin-protein ligase TRIM13 Proteins 0.000 description 8
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 8
- 241000699666 Mus <mouse, genus> Species 0.000 description 8
- 125000003275 alpha amino acid group Chemical group 0.000 description 8
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 8
- 230000002255 enzymatic effect Effects 0.000 description 8
- 239000000499 gel Substances 0.000 description 8
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical compound O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 8
- 239000000126 substance Substances 0.000 description 8
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 8
- 238000001962 electrophoresis Methods 0.000 description 7
- 238000003780 insertion Methods 0.000 description 7
- 230000037431 insertion Effects 0.000 description 7
- 238000002955 isolation Methods 0.000 description 7
- 238000011160 research Methods 0.000 description 7
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 6
- KDCGOANMDULRCW-UHFFFAOYSA-N 7H-purine Chemical compound N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- 239000007995 HEPES buffer Substances 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 108020001507 fusion proteins Proteins 0.000 description 6
- 102000037865 fusion proteins Human genes 0.000 description 6
- 102000012410 DNA Ligases Human genes 0.000 description 5
- 108010061982 DNA Ligases Proteins 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 5
- 229930182817 methionine Natural products 0.000 description 5
- 102000039446 nucleic acids Human genes 0.000 description 5
- 108020004707 nucleic acids Proteins 0.000 description 5
- 150000007523 nucleic acids Chemical class 0.000 description 5
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 238000013518 transcription Methods 0.000 description 5
- 230000035897 transcription Effects 0.000 description 5
- 238000013519 translation Methods 0.000 description 5
- 229930024421 Adenine Natural products 0.000 description 4
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 4
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 4
- 229910019142 PO4 Inorganic materials 0.000 description 4
- 229920005654 Sephadex Polymers 0.000 description 4
- 239000012507 Sephadex™ Substances 0.000 description 4
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 4
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 4
- 241000700605 Viruses Species 0.000 description 4
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 4
- 229960000643 adenine Drugs 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 229940104302 cytosine Drugs 0.000 description 4
- 230000002068 genetic effect Effects 0.000 description 4
- OKKJLVBELUTLKV-UHFFFAOYSA-N methanol Substances OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 4
- 239000010452 phosphate Substances 0.000 description 4
- 229920002401 polyacrylamide Polymers 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 229940113082 thymine Drugs 0.000 description 4
- 230000003612 virological effect Effects 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- CZPWVGJYEJSRLH-UHFFFAOYSA-N Pyrimidine Chemical compound C1=CN=CN=C1 CZPWVGJYEJSRLH-UHFFFAOYSA-N 0.000 description 3
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 3
- 230000027455 binding Effects 0.000 description 3
- 238000009835 boiling Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 230000000875 corresponding effect Effects 0.000 description 3
- 238000010348 incorporation Methods 0.000 description 3
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 3
- 235000021317 phosphate Nutrition 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 239000002157 polynucleotide Substances 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 229920002477 rna polymer Polymers 0.000 description 3
- RMVRSNDYEFQCLF-UHFFFAOYSA-N thiophenol Chemical compound SC1=CC=CC=C1 RMVRSNDYEFQCLF-UHFFFAOYSA-N 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- VNDYJBBGRKZCSX-UHFFFAOYSA-L zinc bromide Chemical compound Br[Zn]Br VNDYJBBGRKZCSX-UHFFFAOYSA-L 0.000 description 3
- -1 2-nitrophenylsulfenyl Chemical class 0.000 description 2
- KIUYPHAMDKDICO-WHFBIAKZSA-N Ala-Asp-Gly Chemical compound C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(O)=O KIUYPHAMDKDICO-WHFBIAKZSA-N 0.000 description 2
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 2
- 108020004638 Circular DNA Proteins 0.000 description 2
- 102100031780 Endonuclease Human genes 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 2
- SAEWJTCJQVZQNZ-IUKAMOBKSA-N Ile-Thr-Asn Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(=O)N)C(=O)O)N SAEWJTCJQVZQNZ-IUKAMOBKSA-N 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- 108010047761 Interferon-alpha Proteins 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- XWEVVRRSIOBJOO-SRVKXCTJSA-N Leu-Pro-Gln Chemical compound [H]N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(O)=O XWEVVRRSIOBJOO-SRVKXCTJSA-N 0.000 description 2
- MUCIDQMDOYQYBR-IHRRRGAJSA-N Leu-Pro-His Chemical compound CC(C)C[C@@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC2=CN=CN2)C(=O)O)N MUCIDQMDOYQYBR-IHRRRGAJSA-N 0.000 description 2
- XGDCYUQSFDQISZ-BQBZGAKWSA-N Leu-Ser Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CO)C(O)=O XGDCYUQSFDQISZ-BQBZGAKWSA-N 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- XNMYNGDKJNOKHH-BZSNNMDCSA-N Phe-Ser-Tyr Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O XNMYNGDKJNOKHH-BZSNNMDCSA-N 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 108010056088 Somatostatin Proteins 0.000 description 2
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 239000000908 ammonium hydroxide Substances 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 230000000202 analgesic effect Effects 0.000 description 2
- 239000004202 carbamide Substances 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000009833 condensation Methods 0.000 description 2
- 230000005494 condensation Effects 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 230000001965 increasing effect Effects 0.000 description 2
- 230000000977 initiatory effect Effects 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 239000013067 intermediate product Substances 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 239000002777 nucleoside Substances 0.000 description 2
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 239000000741 silica gel Substances 0.000 description 2
- 229910002027 silica gel Inorganic materials 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 238000012795 verification Methods 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- ASJSAQIRZKANQN-CRCLSJGQSA-N 2-deoxy-D-ribose Chemical group OC[C@@H](O)[C@@H](O)CC=O ASJSAQIRZKANQN-CRCLSJGQSA-N 0.000 description 1
- AYKYXWQEBUNJCN-UHFFFAOYSA-N 3-methylfuran-2,5-dione Chemical compound CC1=CC(=O)OC1=O AYKYXWQEBUNJCN-UHFFFAOYSA-N 0.000 description 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- PAIHPOGPJVUFJY-WDSKDSINSA-N Ala-Glu-Gly Chemical compound C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(O)=O PAIHPOGPJVUFJY-WDSKDSINSA-N 0.000 description 1
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
- 239000005695 Ammonium acetate Substances 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108091032955 Bacterial small RNA Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-M Bicarbonate Chemical compound OC([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-M 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000009025 Endorphins Human genes 0.000 description 1
- 108010049140 Endorphins Proteins 0.000 description 1
- 108091029865 Exogenous DNA Proteins 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 101000632994 Homo sapiens Somatostatin Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- ZMJBYMUCKBYSCP-UHFFFAOYSA-N Hydroxycitric acid Chemical compound OC(=O)C(O)C(O)(C(O)=O)CC(O)=O ZMJBYMUCKBYSCP-UHFFFAOYSA-N 0.000 description 1
- QGXQHJQPAPMACW-PPCPHDFISA-N Ile-Thr-Lys Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCCN)C(=O)O)N QGXQHJQPAPMACW-PPCPHDFISA-N 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 102000006992 Interferon-alpha Human genes 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241000283956 Manis Species 0.000 description 1
- IHRFZLQEQVHXFA-RHYQMDGZSA-N Met-Thr-Lys Chemical compound CSCC[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](C(O)=O)CCCCN IHRFZLQEQVHXFA-RHYQMDGZSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 101500024096 Mus musculus Corticotropin Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 241001467460 Myxogastria Species 0.000 description 1
- 101100205189 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) leu-5 gene Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108010076181 Proinsulin Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 1
- 101150039863 Rich gene Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 102000005157 Somatostatin Human genes 0.000 description 1
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- YFOCMOVJBQDBCE-NRPADANISA-N Val-Ala-Glu Chemical compound C[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)[C@H](C(C)C)N YFOCMOVJBQDBCE-NRPADANISA-N 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- XQJHRCVXRAJIDY-UHFFFAOYSA-N aminophosphine Chemical compound PN XQJHRCVXRAJIDY-UHFFFAOYSA-N 0.000 description 1
- 235000019257 ammonium acetate Nutrition 0.000 description 1
- 229940043376 ammonium acetate Drugs 0.000 description 1
- 239000000730 antalgic agent Substances 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000000712 assembly Effects 0.000 description 1
- 238000000429 assembly Methods 0.000 description 1
- 230000003190 augmentative effect Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 150000001732 carboxylic acid derivatives Chemical group 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 208000037516 chromosome inversion disease Diseases 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 239000013058 crude material Substances 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000006642 detritylation reaction Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 101150016518 for gene Proteins 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 238000010359 gene isolation Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 230000008570 general process Effects 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 102000045305 human SST Human genes 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- AFQIYTIJXGTIEY-UHFFFAOYSA-N hydrogen carbonate;triethylazanium Chemical compound OC(O)=O.CCN(CC)CC AFQIYTIJXGTIEY-UHFFFAOYSA-N 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- LYGJENNIWJXYER-UHFFFAOYSA-N nitromethane Chemical compound C[N+]([O-])=O LYGJENNIWJXYER-UHFFFAOYSA-N 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 230000001817 pituitary effect Effects 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 230000003334 potential effect Effects 0.000 description 1
- 230000000063 preceeding effect Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 125000000548 ribosyl group Chemical group C1([C@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 description 1
- 229960000553 somatostatin Drugs 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 230000009897 systematic effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000005026 transcription initiation Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000000844 transformation Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 229960004799 tryptophan Drugs 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 229940035893 uracil Drugs 0.000 description 1
- 238000010792 warming Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H21/00—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/665—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans derived from pro-opiomelanocortin, pro-enkephalin or pro-dynorphin
- C07K14/675—Beta-endorphins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/58—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving labelled substances
- G01N33/60—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving labelled substances involving radioactive labelled substances
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Zoology (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Wood Science & Technology (AREA)
- Urology & Nephrology (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Hematology (AREA)
- Crystallography & Structural Chemistry (AREA)
- Analytical Chemistry (AREA)
- Cell Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Plant Pathology (AREA)
- Food Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Saccharide Compounds (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US375,493 | 1982-05-06 | ||
| US06/375,493 US4652639A (en) | 1982-05-06 | 1982-05-06 | Manufacture and expression of structural genes |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1266628A true CA1266628A (fr) | 1990-03-13 |
Family
ID=23481109
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA000427371A Expired - Lifetime CA1266628A (fr) | 1982-05-06 | 1983-05-04 | Fabrication et expression de genes structuraux |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US4652639A (fr) |
| EP (1) | EP0108787B1 (fr) |
| JP (1) | JPH0789934B2 (fr) |
| CA (1) | CA1266628A (fr) |
| DE (1) | DE3381438D1 (fr) |
| IL (1) | IL68491A (fr) |
| IT (1) | IT1212983B (fr) |
| WO (1) | WO1983004029A1 (fr) |
Families Citing this family (107)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6936694B1 (en) | 1982-05-06 | 2005-08-30 | Intermune, Inc. | Manufacture and expression of large structural genes |
| US4652639A (en) * | 1982-05-06 | 1987-03-24 | Amgen | Manufacture and expression of structural genes |
| US7138505B1 (en) | 1984-01-12 | 2006-11-21 | Novartis Vaccines And Diagnostics, Inc. | Factor VIII:C nucleic acid molecules |
| US6291662B1 (en) | 1984-12-05 | 2001-09-18 | Amgen Inc. | Recombinant methods for production of serine protease inhibitors and DNA sequences |
| US5871956A (en) * | 1984-12-06 | 1999-02-16 | Amgen Inc. | Recombinant methods for production of serine inhibitors and DNA sequences useful for same |
| US5900400A (en) * | 1984-12-06 | 1999-05-04 | Amgen Inc. | Serine protease inhibitor analogs |
| US6132990A (en) * | 1984-12-06 | 2000-10-17 | Amgen Boulder Inc. | Recombinant methods for production of serine protease inhibitors and DNA sequences useful for same |
| US6018030A (en) | 1986-11-04 | 2000-01-25 | Protein Polymer Technologies, Inc. | Peptides comprising repetitive units of amino acids and DNA sequences encoding the same |
| US4835260A (en) * | 1987-03-20 | 1989-05-30 | Genetics Institute, Inc. | Erythropoietin composition |
| WO1989009780A1 (fr) * | 1988-04-15 | 1989-10-19 | Chemical Industry Institute Of Toxicology | Oligodesoxynucleotides marques au tritium specifiques a un site |
| US5594113A (en) * | 1988-06-23 | 1997-01-14 | Associates Of Cape Cod, Inc. | Endotoxin binding and neutralizing protein and uses thereof |
| US6043057A (en) * | 1988-09-16 | 2000-03-28 | Vitec Aktiebolag | Recombinant systems for expression of the cholera B-sub-unit with the aid of foreign promoters and/or leader peptides |
| US5268276A (en) * | 1988-09-16 | 1993-12-07 | Jan Holmgren | Recombinant systems for expression of cholera B-sub-unit with the aid of foreign promoters and/or leader peptides |
| ATE123303T1 (de) * | 1988-10-13 | 1995-06-15 | Fujisawa Pharmaceutical Co | D-aminosäureoxidase. |
| US5766939A (en) * | 1989-05-05 | 1998-06-16 | Baylor College Of Medicine | Production of recombinant lactoferrin and lactoferrin polypeptides using CDNA sequences in various organisms |
| US6100054A (en) * | 1989-05-05 | 2000-08-08 | Baylor College Of Medicine | Production for recombinant lactoferrin and lactoferrin polypeptides using DNA sequences in various organisms |
| IL94183A (en) | 1989-05-05 | 2003-09-17 | Baylor College Medicine | cDNA SEQUENCE CODING FOR HUMAN LACTOFERRIN PROTEIN OR PORTION THEREOF AND LACTOFERRIN PROTEIN PRODUCED FROM SAID SEQUENCE |
| US5571697A (en) * | 1989-05-05 | 1996-11-05 | Baylor College Of Medicine Texas Medical Center | Expression of processed recombinant lactoferrin and lactoferrin polypeptide fragments from a fusion product in Aspergillus |
| US5571691A (en) * | 1989-05-05 | 1996-11-05 | Baylor College Of Medicine | Production of recombinant lactoferrin and lactoferrin polypeptides using CDNA sequences in various organisms |
| US5849881A (en) * | 1989-05-05 | 1998-12-15 | Baylor College Medicine | Production of recombinant lactoferrin and lactoferrin polypeptides using cDNA sequences in various organisms |
| US5807828A (en) * | 1989-06-16 | 1998-09-15 | Cor Therapeutics, Inc. | Platelet aggregation inhibitors |
| JP2527035B2 (ja) * | 1989-06-16 | 1996-08-21 | 東洋紡績株式会社 | クレアチニン・アミドヒドロラ―ゼをコ―ドする遺伝子を含有するdna断片、該dna断片を有する組換えベクタ―及び該組換えベクタ―を有する形質転換体、並びにクレアチニン・アミドヒドロラ―ゼの製造方法 |
| US5318899A (en) * | 1989-06-16 | 1994-06-07 | Cor Therapeutics, Inc. | Platelet aggregation inhibitors |
| US5686570A (en) * | 1989-06-16 | 1997-11-11 | Cor Therapeutics, Inc. | Platelet aggregation inhibitors |
| US5627262A (en) * | 1989-07-05 | 1997-05-06 | The Board Of Regents Of The University Of Oklahoma | Method and composition for the treatment of septic shock |
| IL95495A (en) * | 1989-08-29 | 1996-10-16 | Hoechst Ag | Fusion proteins their preparation and use |
| US5358857A (en) * | 1989-08-29 | 1994-10-25 | The General Hospital Corp. | Method of preparing fusion proteins |
| US5227293A (en) * | 1989-08-29 | 1993-07-13 | The General Hospital Corporation | Fusion proteins, their preparation and use |
| DK16490D0 (da) * | 1990-01-19 | 1990-01-19 | Novo Nordisk As | Enzym |
| IL97311A0 (en) * | 1990-02-23 | 1992-05-25 | Lilly Co Eli | Vectors and compounds for expression of glycosylation mutants of human protein c |
| US5322785A (en) * | 1990-04-26 | 1994-06-21 | New England Biolabs, Inc. | Purified thermostable DNA polymerase obtainable from thermococcus litoralis |
| US5756334A (en) * | 1990-04-26 | 1998-05-26 | New England Biolabs, Inc. | Thermostable DNA polymerase from 9°N-7 and methods for producing the same |
| US5500363A (en) * | 1990-04-26 | 1996-03-19 | New England Biolabs, Inc. | Recombinant thermostable DNA polymerase from archaebacteria |
| US5352778A (en) * | 1990-04-26 | 1994-10-04 | New England Biolabs, Inc. | Recombinant thermostable DNA polymerase from archaebacteria |
| US5670350A (en) * | 1990-08-20 | 1997-09-23 | Novartis Finance Corporation | Genomic DNA encoding a pseudomonas global transcriptional activation element and its use in activating gene expression |
| US5244796A (en) * | 1990-10-12 | 1993-09-14 | Syracuse University | Cloned leuconostoc mesenteroides glucose-6-phosphate dehydrogenase genes and method of making glucose-6-phospate dehydrogenase |
| JP4236698B2 (ja) * | 1990-11-26 | 2009-03-11 | ジェネティックス インスティチュート,リミテッド ライアビリティ カンパニー | 宿主細胞でのpaceの発現およびその使用法 |
| JP3483880B2 (ja) * | 1991-04-02 | 2004-01-06 | ノボザイムス アクティーゼルスカブ | キシラナーゼ、これに対応する組み換えdna配列、キシラナーゼ含有剤、及びこの剤の使用 |
| US5876985A (en) * | 1991-04-25 | 1999-03-02 | Board Of Regents, The University Of Texas System | Methods and compositions for the preparation of recombinant Trichomonas vaginalis proteins and peptides |
| DE4117747A1 (de) * | 1991-05-30 | 1992-12-03 | Bayer Ag | Kaffeoyl-coa 3-o-methyltransferase-gene |
| DE4208277A1 (de) * | 1992-03-13 | 1993-09-16 | Bosch Gmbh Robert | Verkehrsrundfunkempfaenger |
| DK42092D0 (fr) * | 1992-03-27 | 1992-03-27 | Novo Nordisk As | |
| US6174666B1 (en) | 1992-03-27 | 2001-01-16 | The United States Of America As Represented By The Department Of Health And Human Services | Method of eliminating inhibitory/instability regions from mRNA |
| ZA932568B (en) * | 1992-04-24 | 1993-11-12 | Baylor College Midecine A Non | Production of recombinant human lactoferrin |
| US5621089A (en) * | 1992-05-27 | 1997-04-15 | Novo Nordisk Biotech, Inc. | Nucleic acid constructs for the production of a Bacillus alkaline protease |
| US6869925B1 (en) * | 1992-09-09 | 2005-03-22 | Amgen Inc. | Inhibition of retrovirus infection |
| US7008783B1 (en) | 1992-09-22 | 2006-03-07 | Maruha Corporation | Gene encoding chondroitinase ABC and uses therefor |
| US5776755A (en) * | 1992-10-09 | 1998-07-07 | Helsinki University Licensing, Ltd. | FLT4, a receptor tyrosine kinase |
| US6107046A (en) * | 1992-10-09 | 2000-08-22 | Orion Corporation | Antibodies to Flt4, a receptor tyrosine kinase and uses thereof |
| US6824777B1 (en) * | 1992-10-09 | 2004-11-30 | Licentia Ltd. | Flt4 (VEGFR-3) as a target for tumor imaging and anti-tumor therapy |
| US5484727A (en) * | 1992-10-14 | 1996-01-16 | Trustees Of Dartmouth College | Cloned gene encoding acylcoenzyme A: cholesterol acyltransferase (ACAT) |
| JPH08503852A (ja) * | 1992-11-25 | 1996-04-30 | ユニバーシティ オブ ピッツバーグ オブ ザ コモンウェルス システム オブハイヤー エデュケーション | ヒト誘導性一酸化窒素シンターゼのcDNAクローンおよびその作製方法 |
| US5712366A (en) * | 1993-05-25 | 1998-01-27 | The United States Of America As Represented By The Secretary Of The Army | Fabrication of nanoscale materials using self-assembling proteins |
| DK72593D0 (da) * | 1993-06-18 | 1993-06-18 | Symbicom Ab | Rekombinant protein |
| US5804558A (en) * | 1993-07-20 | 1998-09-08 | University Of California | Protegrins |
| US6159936A (en) * | 1993-07-20 | 2000-12-12 | The Regents Of The University Of California | Compositions and methods for treating and preventing microbial and viral infections |
| US5693486A (en) * | 1993-07-20 | 1997-12-02 | Intrabiotics | DNA sequences encoding protegrins and protegrin analogs and their use in recombinant methods of producing protegrins |
| US6653442B1 (en) | 1993-07-20 | 2003-11-25 | Intrabiotics Pharmaceuticals, Inc. | Protegrins |
| US5616485A (en) * | 1993-12-23 | 1997-04-01 | Cangene Corporation | Streptomyces proteases and improved streptomyces strains for expression of peptides and polypeptides |
| US6001604A (en) * | 1993-12-29 | 1999-12-14 | Bio-Technology General Corp. | Refolding of proinsulins without addition of reducing agents |
| US6017880A (en) * | 1994-03-09 | 2000-01-25 | Amgen Inc. | Inhibition of retrovirus infection |
| JP3198842B2 (ja) * | 1994-03-24 | 2001-08-13 | トヨタ自動車株式会社 | ゲラニルゲラニル二リン酸合成酵素およびそれをコードするdna |
| US5786464C1 (en) * | 1994-09-19 | 2012-04-24 | Gen Hospital Corp | Overexpression of mammalian and viral proteins |
| US5795737A (en) * | 1994-09-19 | 1998-08-18 | The General Hospital Corporation | High level expression of proteins |
| US5741898A (en) * | 1994-09-22 | 1998-04-21 | Hanley; Kathleen Marie | DNA sequence encoding nicotiana squalene synthetase |
| JP2938352B2 (ja) * | 1994-09-30 | 1999-08-23 | オリエンタル酵母工業株式会社 | 組換え人マトリライシンの製造方法 |
| EP1353952B1 (fr) | 1994-11-14 | 2007-04-11 | Ludwig Institute For Cancer Research | Flt4 (vegfr-3) utilise comme cible pour l'imagerie des tumeurs et le traitement antitumoral |
| IT1275909B1 (it) * | 1995-03-07 | 1997-10-24 | Mirella Pilone | Frammento di dna codificante d-amminoacido ossidasi |
| US5646025A (en) * | 1995-05-05 | 1997-07-08 | Novo Nordisk A/S | Scytalidium catalase gene |
| US6025326A (en) * | 1995-07-07 | 2000-02-15 | Intrabiotics Pharmaceuticals, Inc. | Compositions and methods for the prevention and treatment of oral mucositis |
| JP3709422B2 (ja) * | 1995-07-21 | 2005-10-26 | 昌 清水 | ニトリラーゼ遺伝子発現に関わる調節因子およびその遺伝子 |
| WO1997014787A1 (fr) * | 1995-10-18 | 1997-04-24 | Novartis Ag | Sequences nucleotidiques codant pour la mevalonate pyrophosphate decarboxylase |
| US5994306A (en) * | 1995-11-22 | 1999-11-30 | Intrabiotics Pharmaceuticals, Inc. | Fine-tuned protegrins |
| US6111081A (en) * | 1996-05-31 | 2000-08-29 | Baylor College Of Medicine | Lactoferrin variants and uses thereof |
| US5916872A (en) * | 1996-07-24 | 1999-06-29 | Intrabiotics Pharmaceuticals, Inc. | Cyclic peptides having broad spectrum antimicrobial activity |
| US6114148C1 (en) * | 1996-09-20 | 2012-05-01 | Gen Hospital Corp | High level expression of proteins |
| US6110668A (en) * | 1996-10-07 | 2000-08-29 | Max-Planck-Gesellschaft Zur Forderung Der Wissenschaften E.V. | Gene synthesis method |
| PT1538206E (pt) * | 1997-09-16 | 2010-04-12 | Centocor Ortho Biotech Inc | Método para a síntese química e construção completa de genes e genomas |
| US6670127B2 (en) | 1997-09-16 | 2003-12-30 | Egea Biosciences, Inc. | Method for assembly of a polynucleotide encoding a target polypeptide |
| AU774266B2 (en) * | 1998-10-09 | 2004-06-24 | Vegenics Limited | Flt4 (VEGFR-3) as a target for tumor imaging and anti-tumor therapy |
| AU2487300A (en) * | 1998-12-31 | 2000-07-31 | Chiron Corporation | Polynucleotides encoding antigenic hiv type c polypeptides, polypeptides and uses thereof |
| ES2299276T3 (es) | 1998-12-31 | 2008-05-16 | Novartis Vaccines And Diagnostics, Inc. | Polipeptidos env del vih modificados. |
| WO2000039302A2 (fr) | 1998-12-31 | 2000-07-06 | Chiron Corporation | Expression amelioree de polypeptides hiv et production de particules de type viral |
| US7935805B1 (en) | 1998-12-31 | 2011-05-03 | Novartis Vaccines & Diagnostics, Inc | Polynucleotides encoding antigenic HIV Type C polypeptides, polypeptides and uses thereof |
| US6107460A (en) * | 1999-03-01 | 2000-08-22 | The Board Of Regents Of The University Of Oklahoma | Antimicrobial peptides and methods of use thereof |
| US8137906B2 (en) * | 1999-06-07 | 2012-03-20 | Sloning Biotechnology Gmbh | Method for the synthesis of DNA fragments |
| AU2001275091A1 (en) | 2000-06-02 | 2001-12-17 | Blue Heron Biotechnology, Inc. | Methods for improving the sequence fidelity of synthetic double-stranded oligonucleotides |
| US20040241650A1 (en) * | 2001-01-19 | 2004-12-02 | Evans Glen A | Computer-directed assembly of a polynucleotide encoding a target polypeptide |
| US7164992B1 (en) | 2001-03-22 | 2007-01-16 | Blue Heron Biotechnology, Inc. | Method and system for polynucleotide synthesis |
| CA2458995C (fr) * | 2001-08-31 | 2013-04-30 | Chiron Corporation | Polynucleotides codant des polypeptides de type b du vih antigeniques, polypeptides et leurs utilisations |
| ATE414767T1 (de) * | 2001-11-22 | 2008-12-15 | Sloning Biotechnology Gmbh | Nukleinsäure-linker und deren verwendung in der gensynthese |
| CN102660564B (zh) | 2004-04-22 | 2013-05-08 | 泰勒克里斯生物治疗学公司 | 重组修饰的纤溶酶 |
| PL2220221T3 (pl) * | 2007-11-29 | 2015-07-31 | Grifols Therapeutics Inc | Rekombinacyjnie zmodyfikowana plazmina |
| US9115352B2 (en) | 2008-03-31 | 2015-08-25 | Sloning Biotechnology Gmbh | Method for the preparation of a nucleic acid library |
| MX2010013282A (es) * | 2008-06-04 | 2010-12-21 | Talecris Biotherapeutics Inc | Composicion, metodo y kit para la preparacion de plasmina. |
| HUE025670T2 (en) | 2009-03-03 | 2016-04-28 | Grifols Therapeutics Inc | A method for producing plasminogen |
| KR101808751B1 (ko) | 2009-11-13 | 2017-12-13 | 그리폴스 테라퓨틱스 인코포레이티드 | 폰 빌레브란트 인자(vWF)-함유 제제, 및 그와 관련된 방법, 키트 및 용도 |
| WO2011150168A1 (fr) | 2010-05-28 | 2011-12-01 | Gen9, Inc. | Procédés et dispositifs de synthèse in situ d'acides nucléiques |
| DE102010056289A1 (de) | 2010-12-24 | 2012-06-28 | Geneart Ag | Verfahren zur Herstellung von Leseraster-korrekten Fragment-Bibliotheken |
| US12595500B2 (en) | 2011-09-26 | 2026-04-07 | Life Technologies Corporation | High efficiency, small volume nucleic acid synthesis |
| CN103945931B (zh) | 2011-09-26 | 2017-03-22 | 基因技术股份公司 | 高效的小体积核酸合成 |
| WO2014153188A2 (fr) | 2013-03-14 | 2014-09-25 | Life Technologies Corporation | Synthèse hautement efficace de petits volumes d'acides nucléiques |
| WO2013093760A2 (fr) | 2011-12-19 | 2013-06-27 | Grifols, S.A. | Compositions, procédés et trousses pour la préparation de protéines recombinantes sialylées |
| WO2013130487A2 (fr) | 2012-02-29 | 2013-09-06 | Duke University | Nouvelles oxydoréductases pour réactions énantiosélectives |
| US10407676B2 (en) | 2014-12-09 | 2019-09-10 | Life Technologies Corporation | High efficiency, small volume nucleic acid synthesis |
| EP3763818A1 (fr) | 2015-10-06 | 2021-01-13 | Pierce Biotechnology, Inc. | Dispositifs et procédés de production de protéines |
| WO2024132094A1 (fr) | 2022-12-19 | 2024-06-27 | Thermo Fisher Scientific Geneart Gmbh | Extraction de molécules d'acide nucléique à séquence vérifiée |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4225784A (en) * | 1976-06-17 | 1980-09-30 | Smith Kline Instruments, Inc. | Covalently bound biological substances to plastic materials and use in radioassay |
| US4140662A (en) * | 1977-03-25 | 1979-02-20 | Ortho Diagnostics, Inc. | Attachment of proteins to inert particles |
| US4366246A (en) * | 1977-11-08 | 1982-12-28 | Genentech, Inc. | Method for microbial polypeptide expression |
| US4322499A (en) * | 1978-12-22 | 1982-03-30 | The Regents Of The University Of California | Adrenocorticotropin-lipotropin precursor gene |
| US4293652A (en) * | 1979-05-25 | 1981-10-06 | Cetus Corporation | Method for synthesizing DNA sequentially |
| US4342832A (en) * | 1979-07-05 | 1982-08-03 | Genentech, Inc. | Method of constructing a replicable cloning vehicle having quasi-synthetic genes |
| US4350764A (en) * | 1980-03-10 | 1982-09-21 | The Regents Of The University Of California | Microbiological synthesis of beta endorphin |
| IE53166B1 (en) * | 1980-08-05 | 1988-08-03 | Searle & Co | Synthetic urogastrone gene,corresponding plasmid recombinants,transformed cells,production thereof and urogastrone expression |
| US4403036A (en) * | 1980-12-02 | 1983-09-06 | University Of Iowa Research Foundation | Genetic reagents for generating plasmids containing multiple copies of DNA segments |
| US6936694B1 (en) * | 1982-05-06 | 2005-08-30 | Intermune, Inc. | Manufacture and expression of large structural genes |
| WO1983004030A1 (fr) * | 1982-05-06 | 1983-11-24 | Applied Molecular Genetics, Inc. | Fabrication et expression de genes pour l'urogastrone et leurs analogues polypeptides |
| US4652639A (en) * | 1982-05-06 | 1987-03-24 | Amgen | Manufacture and expression of structural genes |
| WO1983004028A1 (fr) * | 1982-05-06 | 1983-11-24 | Applied Molecular Genetics, Inc. | Fabrication et expression de genes pour la calcitonine et ses analogues de polypeptide |
-
1982
- 1982-05-06 US US06/375,493 patent/US4652639A/en not_active Expired - Lifetime
-
1983
- 1983-04-15 EP EP83901773A patent/EP0108787B1/fr not_active Expired - Lifetime
- 1983-04-15 DE DE8383901773T patent/DE3381438D1/de not_active Expired - Lifetime
- 1983-04-15 WO PCT/US1983/000563 patent/WO1983004029A1/fr not_active Ceased
- 1983-04-15 JP JP58501807A patent/JPH0789934B2/ja not_active Expired - Lifetime
- 1983-04-26 IL IL68491A patent/IL68491A/xx not_active IP Right Cessation
- 1983-05-04 CA CA000427371A patent/CA1266628A/fr not_active Expired - Lifetime
- 1983-05-04 IT IT8367481A patent/IT1212983B/it active
Also Published As
| Publication number | Publication date |
|---|---|
| IT1212983B (it) | 1989-12-07 |
| EP0108787A4 (fr) | 1986-11-07 |
| IL68491A (en) | 1990-07-26 |
| EP0108787A1 (fr) | 1984-05-23 |
| WO1983004029A1 (fr) | 1983-11-24 |
| IL68491A0 (en) | 1983-07-31 |
| JPS59501096A (ja) | 1984-06-28 |
| JPH0789934B2 (ja) | 1995-10-04 |
| DE3381438D1 (de) | 1990-05-17 |
| EP0108787B1 (fr) | 1990-04-11 |
| IT8367481A0 (it) | 1983-05-04 |
| US4652639A (en) | 1987-03-24 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA1266628A (fr) | Fabrication et expression de genes structuraux | |
| EP0108128B1 (fr) | (Met-1,des-Cys1,des-Tyr2,des-Cys3) interféron gamma humain et séquence d'ADN qui le code | |
| CA1340872C (fr) | Expression microbienne de l'interleukine ii | |
| EP0095350A2 (fr) | Un procédé pour la préparation d'un polypeptide semblable au gamma interféron humain | |
| GB2162851A (en) | beta -urogastrone gene | |
| WO1983004028A1 (fr) | Fabrication et expression de genes pour la calcitonine et ses analogues de polypeptide | |
| EP0163603B1 (fr) | Facteur humain de croissance de cellule-T | |
| JPH0712312B2 (ja) | 改良された抗生物質耐性遺伝子 | |
| AU583018B2 (en) | Gibbon interleukin | |
| JPS59501095A (ja) | カルシトニンおよびその類似体のための遺伝子の製造と発現 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MKEX | Expiry |